Aspartate aminotransferase: Investigation of the active sites
An investigation of the crystal structure of cytosolic pigheart aspartate aminotransferase (AAT, E.C.2.6.1.1) was carried out to determine the structural requirements for ligand recognition by the active site. Structural differences were observed between the two active sites of the AAT dimer. The na...
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| Veröffentlicht in: | Journal of molecular graphics 1990-06, Vol.8 (2), p.111-115 |
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| container_title | Journal of molecular graphics |
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| creator | Nero, T.L. Wong, M.G. Oliver, S.W. Iskander, M.N. Andrews, P.R. |
| description | An investigation of the crystal structure of cytosolic pigheart aspartate aminotransferase (AAT, E.C.2.6.1.1) was carried out to determine the structural requirements for ligand recognition by the active site. Structural differences were observed between the two active sites of the AAT dimer. The natural ligand,
l-aspartate, was docked into both active sites using various methods. However, due to structural differences, the ligand was able to form all the necessary interactions for initial binding in only one of the active sites. The program GRID (P. J. Goodford. J. Med. Chem. 1985,
28, 849-857) was used to predict favorable binding sites for the functional groups of the aspartate ligand. These binding sites corresponded to the position of the docked aspartate ligand, indicating that substrate recognition takes place before any major conformational changes occur within the enzyme. |
| doi_str_mv | 10.1016/0263-7855(90)80091-S |
| format | Article |
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l-aspartate, was docked into both active sites using various methods. However, due to structural differences, the ligand was able to form all the necessary interactions for initial binding in only one of the active sites. The program GRID (P. J. Goodford. J. Med. Chem. 1985,
28, 849-857) was used to predict favorable binding sites for the functional groups of the aspartate ligand. These binding sites corresponded to the position of the docked aspartate ligand, indicating that substrate recognition takes place before any major conformational changes occur within the enzyme.</description><identifier>ISSN: 0263-7855</identifier><identifier>DOI: 10.1016/0263-7855(90)80091-S</identifier><identifier>PMID: 2282353</identifier><language>eng</language><publisher>United States: Elsevier B.V</publisher><subject>Animals ; aspartate aminotransferase ; Aspartate Aminotransferases - chemistry ; Aspartate Aminotransferases - metabolism ; Aspartic Acid - metabolism ; binding site predictions ; Binding Sites ; Chickens ; Computer Graphics ; computer programmes ; computer-graphic modeling ; Cytosol - enzymology ; GRID ; ligand docking ; Myocardium - enzymology ; Protein Conformation ; Swine ; X-ray crystallography</subject><ispartof>Journal of molecular graphics, 1990-06, Vol.8 (2), p.111-115</ispartof><rights>1990</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-fa946a306964466cc4dcd02085a6c3f59eafceaba7a12400fd5164515d3e98223</citedby><cites>FETCH-LOGICAL-c357t-fa946a306964466cc4dcd02085a6c3f59eafceaba7a12400fd5164515d3e98223</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2282353$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nero, T.L.</creatorcontrib><creatorcontrib>Wong, M.G.</creatorcontrib><creatorcontrib>Oliver, S.W.</creatorcontrib><creatorcontrib>Iskander, M.N.</creatorcontrib><creatorcontrib>Andrews, P.R.</creatorcontrib><title>Aspartate aminotransferase: Investigation of the active sites</title><title>Journal of molecular graphics</title><addtitle>J Mol Graph</addtitle><description>An investigation of the crystal structure of cytosolic pigheart aspartate aminotransferase (AAT, E.C.2.6.1.1) was carried out to determine the structural requirements for ligand recognition by the active site. Structural differences were observed between the two active sites of the AAT dimer. The natural ligand,
l-aspartate, was docked into both active sites using various methods. However, due to structural differences, the ligand was able to form all the necessary interactions for initial binding in only one of the active sites. The program GRID (P. J. Goodford. J. Med. Chem. 1985,
28, 849-857) was used to predict favorable binding sites for the functional groups of the aspartate ligand. These binding sites corresponded to the position of the docked aspartate ligand, indicating that substrate recognition takes place before any major conformational changes occur within the enzyme.</description><subject>Animals</subject><subject>aspartate aminotransferase</subject><subject>Aspartate Aminotransferases - chemistry</subject><subject>Aspartate Aminotransferases - metabolism</subject><subject>Aspartic Acid - metabolism</subject><subject>binding site predictions</subject><subject>Binding Sites</subject><subject>Chickens</subject><subject>Computer Graphics</subject><subject>computer programmes</subject><subject>computer-graphic modeling</subject><subject>Cytosol - enzymology</subject><subject>GRID</subject><subject>ligand docking</subject><subject>Myocardium - enzymology</subject><subject>Protein Conformation</subject><subject>Swine</subject><subject>X-ray crystallography</subject><issn>0263-7855</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9LAzEQxXNQaq1-A4U9iR5Wk2yS3QgKpfinUPBQPYdpdqKR7m5N0oLf3q0tHj0NzLz3ZuZHyBmj14wydUO5KvKykvJS06uKUs3y-QEZ_rWPyHGMn5RSVcpqQAacV7yQxZDcjeMKQoKEGTS-7VKANjoMEPE2m7YbjMm_Q_Jdm3UuSx-9zCa_wSz6hPGEHDpYRjzd1xF5e3x4nTzns5en6WQ8y20hy5Q70EJBQZVWQihlrahtTTmtJChbOKkRnEVYQAmMC0pdLZkSksm6QF1xXozIxS53FbqvdX-TaXy0uFxCi906GiaVEkzrXih2Qhu6GAM6swq-gfBtGDVbUmaLxGyRGE3NLykz723n-_z1osH6z7TH1M_vd3Psn9x4DCZaj63F2ge0ydSd_3_BD7N9efw</recordid><startdate>19900601</startdate><enddate>19900601</enddate><creator>Nero, T.L.</creator><creator>Wong, M.G.</creator><creator>Oliver, S.W.</creator><creator>Iskander, M.N.</creator><creator>Andrews, P.R.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>19900601</creationdate><title>Aspartate aminotransferase: Investigation of the active sites</title><author>Nero, T.L. ; Wong, M.G. ; Oliver, S.W. ; Iskander, M.N. ; Andrews, P.R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-fa946a306964466cc4dcd02085a6c3f59eafceaba7a12400fd5164515d3e98223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Animals</topic><topic>aspartate aminotransferase</topic><topic>Aspartate Aminotransferases - chemistry</topic><topic>Aspartate Aminotransferases - metabolism</topic><topic>Aspartic Acid - metabolism</topic><topic>binding site predictions</topic><topic>Binding Sites</topic><topic>Chickens</topic><topic>Computer Graphics</topic><topic>computer programmes</topic><topic>computer-graphic modeling</topic><topic>Cytosol - enzymology</topic><topic>GRID</topic><topic>ligand docking</topic><topic>Myocardium - enzymology</topic><topic>Protein Conformation</topic><topic>Swine</topic><topic>X-ray crystallography</topic><toplevel>online_resources</toplevel><creatorcontrib>Nero, T.L.</creatorcontrib><creatorcontrib>Wong, M.G.</creatorcontrib><creatorcontrib>Oliver, S.W.</creatorcontrib><creatorcontrib>Iskander, M.N.</creatorcontrib><creatorcontrib>Andrews, P.R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of molecular graphics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nero, T.L.</au><au>Wong, M.G.</au><au>Oliver, S.W.</au><au>Iskander, M.N.</au><au>Andrews, P.R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aspartate aminotransferase: Investigation of the active sites</atitle><jtitle>Journal of molecular graphics</jtitle><addtitle>J Mol Graph</addtitle><date>1990-06-01</date><risdate>1990</risdate><volume>8</volume><issue>2</issue><spage>111</spage><epage>115</epage><pages>111-115</pages><issn>0263-7855</issn><abstract>An investigation of the crystal structure of cytosolic pigheart aspartate aminotransferase (AAT, E.C.2.6.1.1) was carried out to determine the structural requirements for ligand recognition by the active site. Structural differences were observed between the two active sites of the AAT dimer. The natural ligand,
l-aspartate, was docked into both active sites using various methods. However, due to structural differences, the ligand was able to form all the necessary interactions for initial binding in only one of the active sites. The program GRID (P. J. Goodford. J. Med. Chem. 1985,
28, 849-857) was used to predict favorable binding sites for the functional groups of the aspartate ligand. These binding sites corresponded to the position of the docked aspartate ligand, indicating that substrate recognition takes place before any major conformational changes occur within the enzyme.</abstract><cop>United States</cop><pub>Elsevier B.V</pub><pmid>2282353</pmid><doi>10.1016/0263-7855(90)80091-S</doi><tpages>5</tpages></addata></record> |
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| ispartof | Journal of molecular graphics, 1990-06, Vol.8 (2), p.111-115 |
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| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Animals aspartate aminotransferase Aspartate Aminotransferases - chemistry Aspartate Aminotransferases - metabolism Aspartic Acid - metabolism binding site predictions Binding Sites Chickens Computer Graphics computer programmes computer-graphic modeling Cytosol - enzymology GRID ligand docking Myocardium - enzymology Protein Conformation Swine X-ray crystallography |
| title | Aspartate aminotransferase: Investigation of the active sites |
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